Abstract
Washed membranes from pea chloroplasts can be resolved into at least 21 protein bands on sodium dodecylsulphate polyacrylamide gels, with molecular weights ranging from 13 000 to over 100 000. Isolated intact pea chloroplasts use both light energy and added ATP to incorporate [ 35S]methionine into six discrete membrane-bound products. Five of these are digestible by pronase, but not by ribonuclease, and have molecular weights of 85 000, 40 000, 32 000, 22 000 and 18 000. These proteins cannot be removed from the membranes by washing with water or EDTA, but can be solubilised by digitonin. The identity of these proteins is unknown, but they do not include cytochrome f, the coupling factor, or Photosystems I and II proteins.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis
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